Pennings S, Meersseman G, Bradbury E M
Department of Biological Chemistry, School of Medicine, University of California, Davis 95616.
Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10275-9. doi: 10.1073/pnas.91.22.10275.
We have previously identified a generally occurring short-range mobility of nucleosome cores on DNA in relatively low ionic strength conditions. Here we report that this mobility of histone octamers positioned on constructs of 5S rDNA is suppressed by the binding of histone H1 or H5 to the nucleosome. Histone H5 is the more potent inhibitor of nucleosome mobility, in accordance with its higher affinity for chromatin. We propose that this reversible restraint on chromatin dynamics may play a role in local regulation of processes that require access to the DNA.
我们之前已经确定,在相对低离子强度条件下,核小体核心在DNA上普遍存在短程移动性。在此我们报告,位于5S rDNA构建体上的组蛋白八聚体的这种移动性会被组蛋白H1或H5与核小体的结合所抑制。根据组蛋白H5对染色质具有更高的亲和力,它是核小体移动性更强的抑制剂。我们提出,这种对染色质动力学的可逆限制可能在需要接触DNA的过程的局部调控中发挥作用。